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KMID : 0545120030130050767
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Journal of Microbiology and Biotechnology
2003 Volume.13 No. 5 p.767 ~ p.772
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Purification and Comparison of Properties of the C-Terminus Truncated Agarase of Pseudomonas sp. W7
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YOON, SOO-CHEOL
LEE, JONG-HEE/AHN, SUN-HEE/LEE, EUN-MI/PARK, EUN-MI/KONG, IN-SOO
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Abstract
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Three plasmids derived from the β-agarase gene (pjaA) of Pseudomonas sp. W7 were expressed in Escherichia coli AD494(DE3) pLysS with lactose as an inducer. These products corresponded to the complete (PjaA) and the two C-terminal truncated (PjaAⅠ and PjaAⅡ) forms of β-agarase. The PjaAⅠ and the PjaAⅡ were originated from exonuclease Ⅲ treatment from PjaA by deleting 127 and 182 amino acid residues-encoded nucleic acids at 3´ region, respectively. The molecular weights of the purified proteins were 71 kDa, 58 kDa, and 50 kDa on SDS-PAGE, respectively. The K_(M) value of PjaAI was lower than that of the PjaA, and the catalytic efficiency (k_(㎝)/K_(M)) of PjaAI was increased to 5 times. The enzyme of PjaAI retained more than 90% activity at 50℃. In contrast to the PjaAI, the remaining activity of the PjaA was only 20% at the same temperature.
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KEYWORD
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